Structural highlights
Publication Abstract from PubMed
Polyketide metabolites produced by modular type I polyketide synthases (PKS) acquire their chemical diversity through the variety of catalytic domains within modules of the pathway. Methyltransferases are among the least characterized of the catalytic domains common to PKS systems. We determined the domain boundaries and characterized the activity of a PKS C-methyltransferase (C-MT) from the curacin A biosynthetic pathway. The C-MT catalyzes S-adenosylmethionine-dependent methyl transfer to the alpha-position of beta-ketoacyl substrates linked to acyl carrier protein (ACP) or a small-molecule analog, but does not act on beta-hydroxyacyl substrates or malonyl-ACP. Key catalytic residues conserved in both bacterial and fungal PKS C-MTs were identified in a 2-A crystal structure and validated biochemically. Analysis of the structure and the sequences bordering the C-MT provides insight into the positioning of this domain within complete PKS modules.
Domain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferase.,Skiba MA, Sikkema AP, Fiers WD, Gerwick WH, Sherman DH, Aldrich CC, Smith JL ACS Chem Biol. 2016 Oct 10. PMID:27723289[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Skiba MA, Sikkema AP, Fiers WD, Gerwick WH, Sherman DH, Aldrich CC, Smith JL. Domain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferase. ACS Chem Biol. 2016 Oct 10. PMID:27723289 doi:http://dx.doi.org/10.1021/acschembio.6b00759
